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Influence of basic residues on dissociation kinetics and dynamics of singly protonated peptides: time-resolved photodissociation study



Product ion yields in postsource decay and time-resolved photodissociation at 193 and 266 nm were measured for some peptide ions with lysine ([KF6 + H]+, [F6K + H]+, and [F3KF3 + H]+) formed by matrix-assisted laser desorption ionization. The critical energy (E0) and entropy (ΔS) were determined by RRKM fitting of the data. The results were similar to those found previously for peptide ions with histidine. To summarize, the presence of a basic residue, histidine or lysine, inside a peptide ion retarded its dissociation by lowering ΔS. On the basis of highly negative ΔS, presence of intramolecular interaction involving a basic group in the transition structure was proposed. Copyright © 2009 John Wiley & Sons, Ltd.